pH-dependent dimerization of spider silk N-terminal domain requires relocation of a wedged tryptophan side chain
about
Carbonic anhydrase generates CO2 and H+ that drive spider silk formation via opposite effects on the terminal domainsSequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formationDiversified Structural Basis of a Conserved Molecular Mechanism for pH-Dependent Dimerization in Spider Silk N-Terminal DomainsCrystal Structure of the Nephila clavipes Major Ampullate Spidroin 1A N-terminal Domain Reveals Plasticity at the Dimer InterfaceEfficient protein production inspired by how spiders make silkFull-length minor ampullate spidroin gene sequence.Spider wrapping silk fibre architecture arising from its modular soluble protein precursor.Mass spectrometry captures structural intermediates in protein fiber self-assemblyEffect of sodium chloride on the structure and stability of spider silk's N-terminal protein domain.Control of amyloid assembly by autoregulation.Toward spinning artificial spider silk.Transmissible amyloid.Electrostatics analysis of the mutational and pH effects of the N-terminal domain self-association of the major ampullate spidroin.Acidic Residues Control the Dimerization of the N-terminal Domain of Black Widow Spiders' Major Ampullate Spidroin 1The N-terminal domains of spider silk proteins assemble ultrafast and protected from charge screening.Conservation of folding and association within a family of spidroin N-terminal domains.Degree of Biomimicry of Artificial Spider Silk Spinning Assessed by NMR Spectroscopy.Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk.Spider silk proteome provides insight into the structural characterization of Nephila clavipes flagelliform spidroinDegree of Biomimicry of Artificial Spider Silk Spinning Assessed by NMR SpectroscopyTwo-step self-assembly of a spider silk molecular clamp
P2860
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P2860
pH-dependent dimerization of spider silk N-terminal domain requires relocation of a wedged tryptophan side chain
description
2012 nî lūn-bûn
@nan
2012 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
pH-dependent dimerization of s ...... a wedged tryptophan side chain
@ast
pH-dependent dimerization of s ...... a wedged tryptophan side chain
@en
pH-dependent dimerization of s ...... a wedged tryptophan side chain
@nl
type
label
pH-dependent dimerization of s ...... a wedged tryptophan side chain
@ast
pH-dependent dimerization of s ...... a wedged tryptophan side chain
@en
pH-dependent dimerization of s ...... a wedged tryptophan side chain
@nl
prefLabel
pH-dependent dimerization of s ...... a wedged tryptophan side chain
@ast
pH-dependent dimerization of s ...... a wedged tryptophan side chain
@en
pH-dependent dimerization of s ...... a wedged tryptophan side chain
@nl
P2093
P50
P3181
P1476
pH-dependent dimerization of s ...... a wedged tryptophan side chain
@en
P2093
Glareh Askarieh
Hans Jörnvall
Kerstin Nordling
My Hedhammar
P304
P3181
P356
10.1016/J.JMB.2012.06.004
P407
P577
2012-09-28T00:00:00Z